ID GPSM1_HUMAN Reviewed; 675 AA. AC Q86YR5; A9Z1X4; B1B0W3; Q86SR5; Q969T1; Q9UFS8; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 2. DT 24-JAN-2024, entry version 158. DE RecName: Full=G-protein-signaling modulator 1; DE AltName: Full=Activator of G-protein signaling 3; GN Name=GPSM1; Synonyms=AGS3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RA Cismowski M.J., Kopatz S.A., Puhl H.L. III, Sharma S.V., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Fetal brain, and Rhabdomyosarcoma; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-675 (ISOFORM 1). RC TISSUE=Mammary cancer; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP FUNCTION. RX PubMed=11024022; DOI=10.1074/jbc.m006478200; RA Natochin M., Lester B., Peterson Y.K., Bernard M.L., Lanier S.M., RA Artemyev N.O.; RT "AGS3 inhibits GDP dissociation from galpha subunits of the Gi family and RT rhodopsin-dependent activation of transducin."; RL J. Biol. Chem. 275:40981-40985(2000). RN [7] RP FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND SUBCELLULAR RP LOCATION. RX PubMed=12642577; DOI=10.1074/jbc.m300917200; RA Pattingre S., de Vries L., Bauvy C., Chantret I., Cluzeaud F., RA Ogier-Denis E., Vandewalle A., Codogno P.; RT "The G-protein regulator AGS3 controls an early event during macroautophagy RT in human intestinal HT-29 cells."; RL J. Biol. Chem. 278:20995-21002(2003). RN [8] RP INTERACTION WITH INSC. RX PubMed=16458856; DOI=10.1016/j.bbrc.2006.01.050; RA Izaki T., Kamakura S., Kohjima M., Sumimoto H.; RT "Two forms of human Inscuteable-related protein that links Par3 to the Pins RT homologues LGN and AGS3."; RL Biochem. Biophys. Res. Commun. 341:1001-1006(2006). RN [9] RP INTERACTION WITH FRMPD1, AND SUBCELLULAR LOCATION. RX PubMed=18566450; DOI=10.1074/jbc.m803497200; RA An N., Blumer J.B., Bernard M.L., Lanier S.M.; RT "The PDZ and band 4.1 containing protein Frmpd1 regulates the subcellular RT location of activator of G-protein signaling 3 and its interaction with G- RT proteins."; RL J. Biol. Chem. 283:24718-24728(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-492 AND SER-493, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-469; SER-471 AND RP SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Guanine nucleotide dissociation inhibitor (GDI) which CC functions as a receptor-independent activator of heterotrimeric G- CC protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form CC thus uncoupling heterotrimeric G-proteins signaling from G protein- CC coupled receptors. Controls spindle orientation and asymmetric cell CC fate of cerebral cortical progenitors. May also be involved in CC macroautophagy in intestinal cells. May play a role in drug addiction. CC {ECO:0000269|PubMed:11024022, ECO:0000269|PubMed:12642577}. CC -!- SUBUNIT: Interacts with GNAI1, GNAI2 and GNAI3 preferentially in their CC GDP-bound state. May also interact with GNAO1. Interacts with CC STK11/LKB1 and MACF1 (By similarity). Interacts with INSC/inscuteable CC and FRMPD1. {ECO:0000250, ECO:0000269|PubMed:16458856, CC ECO:0000269|PubMed:18566450}. CC -!- INTERACTION: CC Q86YR5-3; O14503: BHLHE40; NbExp=3; IntAct=EBI-10261098, EBI-711810; CC Q86YR5-3; Q8TEB1: DCAF11; NbExp=3; IntAct=EBI-10261098, EBI-2213388; CC Q86YR5-3; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-10261098, EBI-9679045; CC Q86YR5-3; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-10261098, EBI-7225287; CC Q86YR5-3; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-10261098, EBI-1384254; CC Q86YR5-3; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-10261098, EBI-6658203; CC Q86YR5-3; O75603: GCM2; NbExp=3; IntAct=EBI-10261098, EBI-10188645; CC Q86YR5-3; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-10261098, EBI-7251368; CC Q86YR5-3; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-10261098, EBI-740641; CC Q86YR5-3; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-10261098, EBI-2556193; CC Q86YR5-3; Q8N443: RIBC1; NbExp=3; IntAct=EBI-10261098, EBI-10265323; CC Q86YR5-3; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-10261098, EBI-693002; CC Q86YR5-3; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-10261098, EBI-745958; CC Q86YR5-3; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-10261098, EBI-750487; CC Q86YR5-3; Q14119: VEZF1; NbExp=3; IntAct=EBI-10261098, EBI-11980193; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum CC membrane; Peripheral membrane protein; Cytoplasmic side. Golgi CC apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell CC membrane; Peripheral membrane protein; Cytoplasmic side. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q86YR5-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=Q86YR5-2; Sequence=VSP_020937; CC Name=3; CC IsoId=Q86YR5-3; Sequence=VSP_020938, VSP_020939; CC Name=4; Synonyms=FL; CC IsoId=Q86YR5-4; Sequence=VSP_039028; CC -!- TISSUE SPECIFICITY: Expressed in intestinal cells. CC {ECO:0000269|PubMed:12642577}. CC -!- DOMAIN: The GoLoco domains mediate interaction with G(i/o) alpha (By CC similarity). The GoLoco domains are essential for the GDI activity CC toward G(i/o) alpha. {ECO:0000250}. CC -!- PTM: Phosphorylation regulates interaction with G(i/o) alpha. CC {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 2]: Minor isoform. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Major isoform. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GPSM family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH09979.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH17353.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAB55951.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY173053; AAO17260.1; -; mRNA. DR EMBL; BX649589; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW88216.1; -; Genomic_DNA. DR EMBL; BC009979; AAH09979.1; ALT_INIT; mRNA. DR EMBL; BC017353; AAH17353.1; ALT_INIT; mRNA. DR EMBL; BC048343; AAH48343.1; -; mRNA. DR EMBL; AL117478; CAB55951.1; ALT_FRAME; mRNA. DR CCDS; CCDS48055.1; -. [Q86YR5-1] DR CCDS; CCDS48056.1; -. [Q86YR5-2] DR CCDS; CCDS6996.2; -. [Q86YR5-3] DR PIR; T17261; T17261. DR RefSeq; NP_001139110.2; NM_001145638.2. DR RefSeq; NP_001139111.1; NM_001145639.1. [Q86YR5-2] DR RefSeq; NP_001186932.1; NM_001200003.1. [Q86YR5-2] DR RefSeq; NP_056412.5; NM_015597.5. DR RefSeq; XP_016870088.1; XM_017014599.1. DR AlphaFoldDB; Q86YR5; -. DR SMR; Q86YR5; -. DR BioGRID; 117539; 64. DR IntAct; Q86YR5; 37. DR MINT; Q86YR5; -. DR STRING; 9606.ENSP00000392828; -. DR iPTMnet; Q86YR5; -. DR MetOSite; Q86YR5; -. DR PhosphoSitePlus; Q86YR5; -. DR BioMuta; GPSM1; -. DR DMDM; 294862435; -. DR EPD; Q86YR5; -. DR jPOST; Q86YR5; -. DR MassIVE; Q86YR5; -. DR MaxQB; Q86YR5; -. DR PaxDb; 9606-ENSP00000392828; -. DR PeptideAtlas; Q86YR5; -. DR ProteomicsDB; 70452; -. [Q86YR5-1] DR ProteomicsDB; 70453; -. [Q86YR5-2] DR ProteomicsDB; 70454; -. [Q86YR5-3] DR ProteomicsDB; 70455; -. [Q86YR5-4] DR Pumba; Q86YR5; -. DR Antibodypedia; 32122; 228 antibodies from 27 providers. DR DNASU; 26086; -. DR Ensembl; ENST00000291775.3; ENSP00000291775.3; ENSG00000160360.13. [Q86YR5-2] DR Ensembl; ENST00000392944.5; ENSP00000376673.1; ENSG00000160360.13. [Q86YR5-2] DR Ensembl; ENST00000429455.5; ENSP00000390705.1; ENSG00000160360.13. [Q86YR5-2] DR GeneID; 26086; -. DR KEGG; hsa:26086; -. DR UCSC; uc004che.3; human. [Q86YR5-1] DR AGR; HGNC:17858; -. DR CTD; 26086; -. DR DisGeNET; 26086; -. DR GeneCards; GPSM1; -. DR HGNC; HGNC:17858; GPSM1. DR HPA; ENSG00000160360; Tissue enhanced (brain). DR MIM; 609491; gene. DR neXtProt; NX_Q86YR5; -. DR OpenTargets; ENSG00000160360; -. DR PharmGKB; PA134986171; -. DR VEuPathDB; HostDB:ENSG00000160360; -. DR eggNOG; KOG1130; Eukaryota. DR GeneTree; ENSGT00940000154667; -. DR HOGENOM; CLU_102588_0_0_1; -. DR InParanoid; Q86YR5; -. DR OrthoDB; 4190321at2759; -. DR PhylomeDB; Q86YR5; -. DR TreeFam; TF328344; -. DR PathwayCommons; Q86YR5; -. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SignaLink; Q86YR5; -. DR BioGRID-ORCS; 26086; 21 hits in 1152 CRISPR screens. DR ChiTaRS; GPSM1; human. DR GeneWiki; GPSM1; -. DR GenomeRNAi; 26086; -. DR Pharos; Q86YR5; Tbio. DR PRO; PR:Q86YR5; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q86YR5; Protein. DR Bgee; ENSG00000160360; Expressed in tibia and 166 other cell types or tissues. DR ExpressionAtlas; Q86YR5; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0001965; F:G-protein alpha-subunit binding; IBA:GO_Central. DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central. DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB. DR GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; IDA:UniProtKB. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0016239; P:positive regulation of macroautophagy; IDA:UniProtKB. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3. DR InterPro; IPR003109; GoLoco_motif. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR45954:SF2; G-PROTEIN-SIGNALING MODULATOR 1; 1. DR PANTHER; PTHR45954; LD33695P; 1. DR Pfam; PF02188; GoLoco; 4. DR Pfam; PF13424; TPR_12; 3. DR SMART; SM00390; GoLoco; 4. DR SMART; SM00028; TPR; 6. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS50877; GOLOCO; 4. DR PROSITE; PS50005; TPR; 6. DR PROSITE; PS50293; TPR_REGION; 2. DR Genevisible; Q86YR5; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cytoplasm; Developmental protein; KW Differentiation; Endoplasmic reticulum; Golgi apparatus; Membrane; KW Methylation; Neurogenesis; Phosphoprotein; Reference proteome; Repeat; KW TPR repeat. FT CHAIN 1..675 FT /note="G-protein-signaling modulator 1" FT /id="PRO_0000252402" FT REPEAT 28..61 FT /note="TPR 1" FT REPEAT 66..99 FT /note="TPR 2" FT REPEAT 106..139 FT /note="TPR 3" FT REPEAT 146..181 FT /note="TPR 4" FT REPEAT 183..202 FT /note="TPR 5" FT REPEAT 209..242 FT /note="TPR 6" FT REPEAT 249..282 FT /note="TPR 7" FT REPEAT 289..322 FT /note="TPR 8" FT REPEAT 329..362 FT /note="TPR 9" FT DOMAIN 495..517 FT /note="GoLoco 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097" FT DOMAIN 548..570 FT /note="GoLoco 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097" FT DOMAIN 596..618 FT /note="GoLoco 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097" FT DOMAIN 630..652 FT /note="GoLoco 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097" FT REGION 1..509 FT /note="Mediates association with membranes" FT /evidence="ECO:0000250" FT REGION 364..487 FT /note="Interaction with STK11/LKB1" FT /evidence="ECO:0000250" FT REGION 391..412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 424..492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 610..630 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 644..675 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 424..440 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 455..474 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 421 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q6IR34" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 469 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 471 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 493 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 545 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R080" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R080" FT VAR_SEQ 1..509 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020937" FT VAR_SEQ 1..23 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_039028" FT VAR_SEQ 404..457 FT /note="ARPKRTQRLSAETWDLLRLPLEREQNGDSHHSGDWRGPSRDSLPLPVRSRKY FT QE -> EFQGCGGVLLPTGTDRIRSCGGVGSRPGQHGGGGSRQKMAPTSQFFLASGTAQ FT A (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020938" FT VAR_SEQ 458..675 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020939" SQ SEQUENCE 675 AA; 74510 MW; 27EB86667EEC1951 CRC64; MAGPAPPVAD ELPGPAARRL YSRMEASCLE LALEGERLCK AGDFKTGVAF FEAAVQVGTE DLKTLSAIYS QLGNAYFYLK EHGRALEYHK HDLLLARTIG DRMGEAKASG NLGNTLKVLG RFDEAAVCCQ RHLSIAQEQG DKVGEARALY NIGNVYHAKG KQLSWNAANA TQDPGHLPPD VRETLCKASE FYERNLSLVK ELGDRAAQGR AYGNLGNTHY LLGNFTEATT FHKERLAIAK EFGDKAAERR AYSNLGNAHV FLGRFDVAAE YYKKTLQLSR QLRDQAVEAQ ACYSLGNTYT LLQDYERAAE YHLRHLLIAQ ELADRVGEGR ACWSLGNAYV SMGRPAQALT FAKKHLQISQ EIGDRHGELT ARMNVAQLQL VLGRLTSPAA SEKPDLAGYE AQGARPKRTQ RLSAETWDLL RLPLEREQNG DSHHSGDWRG PSRDSLPLPV RSRKYQEGPD AERRPREGSH SPLDSADVRV HVPRTSIPRA PSSDEECFFD LLTKFQSSRM DDQRCPLDDG QAGAAEATAA PTLEDRIAQP SMTASPQTEE FFDLIASSQS RRLDDQRASV GSLPGLRITH SNAGHLRGHG EPQEPGDDFF NMLIKYQSSR IDDQRCPPPD VLPRGPTMPD EDFFSLIQRV QAKRMDEQRV DLAGGPEQGA GGPPEPQQQC QPGAS //